RPOB_SHEWM
ID RPOB_SHEWM Reviewed; 1343 AA.
AC B1KMZ0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=Swoo_4697;
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01321};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; CP000961; ACA88947.1; -; Genomic_DNA.
DR RefSeq; WP_012327266.1; NC_010506.1.
DR AlphaFoldDB; B1KMZ0; -.
DR SMR; B1KMZ0; -.
DR STRING; 392500.Swoo_4697; -.
DR EnsemblBacteria; ACA88947; ACA88947; Swoo_4697.
DR KEGG; swd:Swoo_4697; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002168; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1343
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141738"
SQ SEQUENCE 1343 AA; 149895 MW; 741758A4DFE20EA5 CRC64;
MVYSYSEKKR IRKDFGKRPQ VLDIPYLLSI QLDSFKKFTD QDPTGERGFE AAFRSVFPIK
SFSGNSELQY VSYKLGEPVF DVKECQIRGV TYSAPLRVKL RMVLYDREAA PGTVKDIKEQ
EVYMGDIPLM TENGTFVING TERVIVSQLH RSPGVFFDHD RGKTHSSGKV LYNARIIPYR
GSWLDFEFDP KDALFVRIDR RRKLAASIIL RALDYSTQDI LDLFFDRVNF KIKKDSLVMD
LVAERLRGET ASYDIKDVEG TIIVEKGRRI TARHIRQLEK SNTTELEVPV DYIVGKISGQ
DYIDPDTGEV LVSANAEMTL EDLAKLSLAG IKEISTLYIN ELDNGAYMSD TLRIDSTTNR
LEALVEIYRM MRPGEPPTKD AAEALFQNLF FSEERYDLSK VGRMKFNRRL GIDDDEGTGI
LSKEDIVAVM KNIITIRNGN DEVDDIDHLG NRRIRSVGEM AENQFRVGLV RVERAVRERL
SLGDLNELMP QDLINAKPIS AAVKEFFGSS QLSQFMDQNN PLSEVTHKRR ISALGPGGLT
RERAGFEVRD VHPTHYGRLC PIETPEGPNI GLINSLASFA RTNSYGFLET PYRKVIDGVV
TDQVDYLSAI EEGRYVIAQA IVDLDENGRM MDELIACRHK GDSTFMGAAD IQYMDVSPQQ
IISVAASLIP FLEHDDANRA LMGANMQRQA VPTLKADKPL VGTGIERTLA VDSGVVVVAK
RGGYIDYVDA SRIVVKVNES ELRPGEAGID IYNLTKYTRS NQNTCINQRP CCAMGDPVVT
GDVLADGPST DLGDLALGQN MRIAFMPWNG YNFEDSILIS ERVAQEDRFT TIHIQELSCI
ARDTKLGSEE ITADIPNVGE SALSKLDESG IVYIGAEVKG GDILVGKVTP KGETQLTPEE
KLLRAIFGEK ASDVKDSSLR VPNSVKGTII DVQVFTRDGV EKDKRAVEIE EMHVRQAKKD
LTEEFQILEE GVYGRARNLL LSAGFNEAQL DAIPRSQLLS QSIDDEGKQT ELEQLAEQHD
ELKADFDKKF EVKRRKITQG DDLAPGVLKI VKVYLAVKRT IQPGDKMAGR HGNKGVISKI
NPVEDMPYDE NGNPIDIVLN PLGVPSRMNI GQVLEVHLGA AAKGIGDKIA AMLEEQRELA
ELRGYIKEVY ELGEEVQQRV DIDSFTDDEV VRLAKNLKGG IPTATPAFDG AKEKEIKEML
ALAGLPTTGQ RKLFDGRTGD EFERQVTVGY MYMLKLNHLV DDKMHARSTG SYSLVTQQPL
GGKAQFGGQR FGEMEVWALE AYGAAYTLQE MLTVKSDDVN GRTNMYKNIV DGNHQMQPGM
PESFNVLLKE IRSLGINIEL DQD
